Data collected at CHESS has resulted in the structure determination of 2 new structures. The first being that of a calcium bound form of the two N-terminal domains of the cell adhesion molecule E-cadherin. The structure was solved by a combination of MAD phasing and real space averaging techniques. Data were collected at the Hg LIII edge on a methyl mercury acetate derivative. The results of this structure have allowed us to explain the role played by calcium in both rigidifying and promoting the dimerization of E-cadherin, an important facet of it ability to promote cell adhesion. The results of this structure have recently been reported in Nature. The second structure was that of the dictyostelium discoideum lectin, discoidin I, in complex with carbohydrate. This calciumbinding lectin was substituted with holmium and solved by the MAD phasing approach. We have just finished building the model and refinement is in progress. This molecule is important in mediating cell-matrix interactions and the structure has clearly revealed that it possesses a number of carbohydrate binding sites. We have also collected data on crystals of FLP and CRE recombinases (or fragments), although on these projects crystal optimization is still in progress.